ID F9FKX1_FUSOF Unreviewed; 541 AA.
AC F9FKX1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_07050 {ECO:0000313|EMBL:EGU82464.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU82464.1};
RN [1] {ECO:0000313|EMBL:EGU82464.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU82464.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU82464.1}.
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DR EMBL; AFQF01002156; EGU82464.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FKX1; -.
DR STRING; 660025.F9FKX1; -.
DR PaxDb; 5507-FOXG_02446P0; -.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR PANTHER; PTHR43183:SF1; HYPOTHETICAL DIHYDROXY-ACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR43183; HYPOTHETICAL DIHYDROXYACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT REGION 506..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 57182 MW; 445360419AE25EA3 CRC64;
MSDPKKTVVN PDYDLDQPIT SKVGLRQGLA SYGDPHFSLF LRKVFIKALG YSEDALSRPI
IGIVNTYSSF NPCHANIPQL IDAVKRGVQL NGGLAIDFPT ISIHESFSSP TSMYLRNLMS
MDTEEMIAAQ PCDAVVLIGG CDKTTPAQLM GGISANKPIL HLVTGPMMPG SHRGVRIGAC
TDCRNNWAKY RAGTLDIEDI SAINDELAPT GGTCGVMGTA STMASILVGL GMMPFAGATA
PAVSATRLRI AEATGGLAVA ACKNVERLRP QALLSRESFL NAITVLQAIG GSTNAVVHLM
AIIGRHPKVA GTITLETIDE IGRKTPLLVD LKPSGDNYMT DFHNSGGMLA LFHELKPLLH
LDALTVTGRT LGEEIAHNSL IPVPRELSVI QPFDKPLYPA SSLVVLKGNL APGGAIMKAS
ASKYRKLLQH TGKAVVFTNS ADMAERIDDP DLDVTPESVL VLQNIGPIGN PGMPEAGMIP
IPRKIASQGV LDMLRLSDGR MSGTAGGTIG LHISPESADP KSPLGIVRNE DPGETQDLPA
S
//
